Linked Life Data

8796369

Source:http://linkedlifedata.com/resource/pubmed/id/8796369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-11-14
pubmed:abstractText
Individuals heterozygous for the apolipoprotein(a) [apo(a)] trait have phenotypes combining two different lipoprotein(a) [La(a)] particle suspecies that are present in plasma at a different concentration. Evaluation of the ability of each of these isoforms to bind to fibrin and affect plasminogen binding is essential to assess the pathogenic role of Lp(a) in these subjects; therefore, fractions containing different ratios of Lp(a) with distinct apo(a) isoforms (e.g. B/S3, S1/S4) were prepared by density gradient ultracentrifugation of plasma, and tested. Lp(a) fractions containing mainly small apo(a) isoforms (either B or S1) showed the highest affinity for fibrin (Kd approximately 150 nmol L-1) and the best competitor activity for plasminogen, whereas fractions containing mainly the high molecular mass isoforms (either S3 or S4) showed the lowest affinities (Kd > or = 500 nmol L-1). An increase in Kd was observed as a function of the relative content in isoforms of high molecular mass in these fractions. This inverse relationship between affinity for fibrin and apo(a) size indicates that Lp(a) subspecies in heterozygotes may have different pathogenic potential. Thus, the antifibrinolytic effect of Lp(a) in heterozygous subjects would depend on the relative concentration of the isoform with the highest affinity for fibrin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2972
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
411-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The antifibrinolytic effect of lipoprotein(a) in heterozygous subjects is modulated by the relative concentration of each of the apolipoprotein(a) isoforms and their affinity for fibrin.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale, INSERM U143, Centre Hospitalier Universitaire de Bicêtre, Paris, France.
pubmed:publicationType
Journal Article, Clinical Trial, Controlled Clinical Trial, Research Support, Non-U.S. Gov't